Protein kinase cAMP-activated catalytic subunit beta (PRKACB)

Protein kinase cAMP-activated catalytic subunit beta (PRKACB) is a serine/threonine protein kinase that functions as the catalytic subunit of cyclic AMP-dependent protein kinase (PKA). It mediates the cellular response to increased cAMP, acting as a key component in signal transduction downstream of G protein-coupled receptor (GPCR) activation. PKA is a tetramer composed of two regulatory subunits and two catalytic subunits; upon cAMP binding, it releases the catalytic PRKACB monomers, which phosphorylate diverse intracellular targets and regulate processes including metabolism, cell cycle progression, proliferation, and differentiation. PRKACB’s clinical relevance is mostly in developmental syndromes, with no direct therapeutic drugs targeting the protein; however, it remains a central player in cAMP-mediated signaling and cellular regulation.

Other names

cAMP-dependent protein kinase catalytic subunit betaPKA C-betaPKACBPKACbprotein kinase A catalytic subunit betaprotein kinase, cAMP-dependent, beta catalytic subunitprotein kinase, cAMP-dependent, catalytic, betabeta-CATALYTIC subunit of PKACAFD2Cat BetaCat βCbPKAPKA C-βprotein kinase cAMP-activated catalytic subunit βprotein kinase, cAMP dependent, catalytic, β

Drugs or molecules that modulate cAMP levels will indirectly affect PRKACB activity (activators of adenylate cyclase, inhibitors of cAMP phosphodiesterases) No approved drugs directly inhibit PRKACB; action is generally via activation (cAMP increase) or inhibition (kinase inhibition) within research or tool compound contexts